The objective of this project is a better understanding of the structure, biosynthesis, and assembly of influenza virus. We will investigate the structure of the oligosaccharides of the hemagglutinin glycoprotein of the various antigenic subtypes of human influenza A viruses, and the peptide sequences to which they are attached. The function of the carbohydrate components of influenza viral glycoproteins will also be studied using particles devoid of carbohydrates, which are produced in the presence of the glycosylation inhibitor tunicamycin. We will undertake studies of the function of the nonstructural (NS) protein in influenza virus replication, including its effects on synthesis of polypeptides and virus-specific RNA. The possible occurrence of trans-membrane effects of antiviral antibody on the assembly of influenza virus will be investigated, and attempts will be made to provide evidence which may explain previous conflicting information on the effects of anti-neuraminidase antibody on virus release. We will determine if the two surface glycoproteins of influenza virus may be modulated independently with bivalent antibody, and if the cellular site of virus maturation may be altered by antibodies, lectins, or neuraminidase.